Structure and Mechanical Properties of Human Trichocyte Keratin Intermediate Filament Protein

This study found that keratins have evolutionarily conserved and domain-selectively enriched amino acids, which likely reflect their unique structural roles, with distinct patterns observed among epidermal, hair, and simple-type epithelial keratins.

This study conducted in situ tensile loading experiments with atomic force microscopy to observe how conditioning treatments affect the tensile response of virgin, chemically damaged, and mechanically damaged Caucasian hair.

Keratin heterodimers are preferred for their specific and structural advantages.

Oxidation changes the structure of hair protein filaments, causing them to compact and rearrange.

This study developed a multiscale model to understand human hair fiber mechanics and found that the yield stress decreases linearly with temperature, supported by both simulations and experimental stretching of hair fibers.

This study reports that expressed mouse type Ia and type IIa trichocyte keratins were successfully assembled into intermediate filaments in vitro, while also suggesting that disulfide bond cross linking enhances their stability.

Hair differentiation starts earlier than thought, involving multiple type-II keratins.

This article reviews the molecular characteristics of human hair keratins, noting their distinct classification from epidermal keratins and the variability in expression that may occur without noticeable hair changes, but reports no new study results.

Human nails contain both skin and hair keratins, each needing different extraction methods.